BMRB Entry 18678
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18678
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Title: NMR structure of the N-terminal RNA Binding domain 1 (RRM1) of the protein RBM10 from Homo sapiens
Deposition date: 2012-08-27 Original release date: 2012-09-17
Authors: Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt
Citation: Serrano, Pedro; Wuthrich, Kurt. "NMR structure of the N-terminal RNA Binding domain 1 (RRM1) of the protein RBM10 from Homo sapiens" Not known ., .-..
Assembly members:
entity, polymer, 91 residues, 10479.927 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: SNIVMLRMLPQAATEDDIRG
QLQSHGVQAREVRLMRNKSS
GQSRGFAFVEFSHLQDATRW
MEANQHSLNILGQKVSMHYS
DPKPKINEDWL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 368 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 627 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM1-RBM10 | 1 |
Entities:
Entity 1, RRM1-RBM10 91 residues - 10479.927 Da.
| 1 | SER | ASN | ILE | VAL | MET | LEU | ARG | MET | LEU | PRO | ||||
| 2 | GLN | ALA | ALA | THR | GLU | ASP | ASP | ILE | ARG | GLY | ||||
| 3 | GLN | LEU | GLN | SER | HIS | GLY | VAL | GLN | ALA | ARG | ||||
| 4 | GLU | VAL | ARG | LEU | MET | ARG | ASN | LYS | SER | SER | ||||
| 5 | GLY | GLN | SER | ARG | GLY | PHE | ALA | PHE | VAL | GLU | ||||
| 6 | PHE | SER | HIS | LEU | GLN | ASP | ALA | THR | ARG | TRP | ||||
| 7 | MET | GLU | ALA | ASN | GLN | HIS | SER | LEU | ASN | ILE | ||||
| 8 | LEU | GLY | GLN | LYS | VAL | SER | MET | HIS | TYR | SER | ||||
| 9 | ASP | PRO | LYS | PRO | LYS | ILE | ASN | GLU | ASP | TRP | ||||
| 10 | LEU |
Samples:
sample_1: RRM1-RBM10, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.220 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G??ntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts